Nucleosome dyad determines the H1 C-terminus collapse on distinct DNA arms

Louro J. A., Boopathi R., Beinsteiner B., Mohideen Patel A. K., Cheng T. C., Angelov D., ...More

Structure, vol.31, no.2, pp.201, 2023 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 31 Issue: 2
  • Publication Date: 2023
  • Doi Number: 10.1016/j.str.2022.12.005
  • Journal Name: Structure
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aerospace Database, BIOSIS, Chemical Abstracts Core, Communication Abstracts, EMBASE, INSPEC, MEDLINE, Metadex, Civil Engineering Abstracts
  • Page Numbers: pp.201
  • Keywords: cryo-EM, linker histone H1, molecular dynamics, nucleosome
  • Dokuz Eylül University Affiliated: Yes


© 2023 Elsevier LtdNucleosomes are symmetric structures. However, binding of linker histones generates an inherently asymmetric H1-nucleosome complex, and whether this asymmetry is transmitted to the overall nucleosome structure, and therefore also to chromatin, is unclear. Efforts to investigate potential asymmetry due to H1s have been hampered by the DNA sequence, which naturally differs in each gyre. To overcome this issue, we designed and analyzed by cryo-EM a nucleosome reconstituted with a palindromic (601L) 197-bp DNA. As in the non-palindromic 601 sequence, H1 restricts linker DNA flexibility but reveals partial asymmetrical unwrapping. However, in contrast to the non-palindromic nucleosome, in the palindromic nucleosome H1 CTD collapses to the proximal linker. Molecular dynamics simulations show that this could be dictated by a slightly tilted orientation of the globular domain (GD) of H1, which could be linked to the DNA sequence of the nucleosome dyad.